P38590 · MSG5_YEAST
- ProteinTyrosine-protein phosphatase MSG5
- GeneMSG5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dual specificity phosphatase that dephosphorylates MAP kinase FUS3 on both a Tyr and a Ser or Thr. Has a role in adaptation to pheromone.
Miscellaneous
Present with 538 molecules/cell in log phase SD medium.
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 319 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | MAP kinase tyrosine phosphatase activity | |
Molecular Function | MAP kinase tyrosine/serine/threonine phosphatase activity | |
Molecular Function | protein tyrosine/serine/threonine phosphatase activity | |
Molecular Function | protein tyrosine/threonine phosphatase activity | |
Biological Process | adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion | |
Biological Process | fungal-type cell wall organization or biogenesis | |
Biological Process | negative regulation of cell wall integrity MAPK cascade | |
Biological Process | negative regulation of MAPK cascade | |
Biological Process | pheromone response MAPK cascade | |
Biological Process | regulation of fungal-type cell wall organization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein phosphatase MSG5
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38590
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 319 | Loss of activity. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 7 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094916 | 1-489 | Tyrosine-protein phosphatase MSG5 | |||
Sequence: MQFHSDKQHLDSKTDIDFKPNSPRSLQNRNTKNLSLDIAALHPLMEFSSPSQDVPGSVKFPSPTPLNLFMKPKPIVLEKCPPKVSPRPTPPSLSMRRSEASIYTLPTSLKNRTVSPSVYTKSSTVSSISKLSSSSPLSSFSEKPHLNRVHSLSVKTKDLKLKGIRGRSQTISGLETSTPISSTREGTLDSTDVNRFSNQKNMQTTLIFPEEDSDLNIDMVHAEIYQRTVYLDGPLLVLPPNLYLYSEPKLEDILSFDLVINVAKEIPNLEFLIPPEMAHKIKYYHIEWTHTSKIVKDLSRLTRIIHTAHSQGKKILVHCQCGVSRSASLIVAYIMRYYGLSLNDAYNKLKGVAKDISPNMGLIFQLMEWGTMLSKNSPGEEGETVHMPEEDDIGNNEVSSTTKSYSSASFRSFPMVTNLSSSPNDSSVNSSEVTPRTPATLTGARTALATERGEDDEHCKSLSQPADSLEASVDNESISTAPEQMMFLP | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 98 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 151 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 178 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By pheromone.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Basic and acidic residues | ||||
Sequence: MQFHSDKQHLDSKTDIDF | ||||||
Region | 1-30 | Disordered | ||||
Sequence: MQFHSDKQHLDSKTDIDFKPNSPRSLQNRN | ||||||
Domain | 233-375 | Tyrosine-protein phosphatase | ||||
Sequence: GPLLVLPPNLYLYSEPKLEDILSFDLVINVAKEIPNLEFLIPPEMAHKIKYYHIEWTHTSKIVKDLSRLTRIIHTAHSQGKKILVHCQCGVSRSASLIVAYIMRYYGLSLNDAYNKLKGVAKDISPNMGLIFQLMEWGTMLSK | ||||||
Region | 375-401 | Disordered | ||||
Sequence: KNSPGEEGETVHMPEEDDIGNNEVSST | ||||||
Compositional bias | 419-444 | Polar residues | ||||
Sequence: LSSSPNDSSVNSSEVTPRTPATLTGA | ||||||
Region | 419-489 | Disordered | ||||
Sequence: LSSSPNDSSVNSSEVTPRTPATLTGARTALATERGEDDEHCKSLSQPADSLEASVDNESISTAPEQMMFLP | ||||||
Compositional bias | 449-463 | Basic and acidic residues | ||||
Sequence: ATERGEDDEHCKSLS | ||||||
Compositional bias | 465-482 | Polar residues | ||||
Sequence: PADSLEASVDNESISTAP |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)54,217
- Last updated1996-10-01 v2
- Checksum0D02380B62EA48DC
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Basic and acidic residues | ||||
Sequence: MQFHSDKQHLDSKTDIDF | ||||||
Sequence conflict | 347-348 | in Ref. 1; BAA04485 | ||||
Sequence: NK → DE | ||||||
Compositional bias | 419-444 | Polar residues | ||||
Sequence: LSSSPNDSSVNSSEVTPRTPATLTGA | ||||||
Compositional bias | 449-463 | Basic and acidic residues | ||||
Sequence: ATERGEDDEHCKSLS | ||||||
Compositional bias | 465-482 | Polar residues | ||||
Sequence: PADSLEASVDNESISTAP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D17548 EMBL· GenBank· DDBJ | BAA04485.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U12141 EMBL· GenBank· DDBJ | AAA99659.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z71329 EMBL· GenBank· DDBJ | CAA95922.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X02561 EMBL· GenBank· DDBJ | CAA26402.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006947 EMBL· GenBank· DDBJ | DAA10492.1 EMBL· GenBank· DDBJ | Genomic DNA |